SHIP1_XENLA
ID SHIP1_XENLA Reviewed; 1019 AA.
AC Q6P4S2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1;
DE EC=3.1.3.86 {ECO:0000250|UniProtKB:Q92835};
DE AltName: Full=Inositol polyphosphate-5-phosphatase D;
DE EC=3.1.3.56 {ECO:0000250|UniProtKB:Q92835};
DE AltName: Full=Phosphatidylinositol-4,5-bisphosphate 5-phosphatase;
DE EC=3.1.3.36 {ECO:0000250|UniProtKB:Q92835};
DE AltName: Full=SH2 domain-containing inositol 5'-phosphatase 1;
DE Short=SH2 domain-containing inositol phosphatase 1;
DE Short=SHIP-1;
GN Name=inpp5d; Synonyms=ship, ship1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically
CC hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate
CC (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively
CC regulating the PI3K (phosphoinositide 3-kinase) pathways. Able also to
CC hydrolyzes the 5-phosphate of phosphatidylinositol-4,5-bisphosphate
CC (PtdIns(4,5)P3) and inositol 1,3,4,5-tetrakisphosphate. Acts as a
CC negative regulator of B-cell antigen receptor signaling. Mediates
CC signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central
CC role in terminating signal transduction from activating
CC immune/hematopoietic cell receptor systems. Acts as a negative
CC regulator of myeloid cell proliferation/survival and chemotaxis, mast
CC cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3
CC signaling in platelets and JNK signaling in B-cells.
CC {ECO:0000250|UniProtKB:Q92835}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:57836; EC=3.1.3.86;
CC Evidence={ECO:0000250|UniProtKB:Q92835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-
CC inositol 1,3,4-trisphosphate + phosphate; Xref=Rhea:RHEA:11392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:58414; EC=3.1.3.56;
CC Evidence={ECO:0000250|UniProtKB:Q92835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000250|UniProtKB:Q92835};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ES52}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9ES52}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9ES52}. Membrane raft
CC {ECO:0000250|UniProtKB:Q9ES52}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9ES52}. Note=Translocates to the plasma
CC membrane when activated, translocation is probably due to different
CC mechanisms depending on the stimulus and cell type.
CC {ECO:0000250|UniProtKB:Q9ES52}.
CC -!- DOMAIN: The SH2 domain interacts with tyrosine phosphorylated forms of
CC proteins. {ECO:0000250|UniProtKB:Q9ES52}.
CC -!- DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated
CC proteins is required for the specific binding of the PID domain.
CC {ECO:0000250|UniProtKB:Q9ES52}.
CC -!- PTM: Tyrosine phosphorylated by the members of the SRC family after
CC exposure to a diverse array of extracellular stimuli.
CC {ECO:0000250|UniProtKB:Q9ES52}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC family. {ECO:0000305}.
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DR EMBL; BC063273; AAH63273.1; -; mRNA.
DR RefSeq; NP_001083668.1; NM_001090199.1.
DR AlphaFoldDB; Q6P4S2; -.
DR SMR; Q6P4S2; -.
DR DNASU; 399051; -.
DR GeneID; 399051; -.
DR KEGG; xla:399051; -.
DR CTD; 399051; -.
DR Xenbase; XB-GENE-6071368; inpp5d.L.
DR OrthoDB; 311217at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 399051; Expressed in spleen and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:RHEA.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR Gene3D; 3.30.505.10; -; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Hydrolase; Immunity;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW SH2 domain; SH3-binding.
FT CHAIN 1..1019
FT /note="Phosphatidylinositol 3,4,5-trisphosphate 5-
FT phosphatase 1"
FT /id="PRO_0000302869"
FT DOMAIN 5..101
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 102..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..125
FT /note="SH3-binding 1"
FT MOTIF 966..971
FT /note="SH3-binding 2"
FT MOTIF 1004..1007
FT /note="NPXY motif"
FT COMPBIAS 910..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1007
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES52"
SQ SEQUENCE 1019 AA; 115297 MW; 6FF3E53E0658E27A CRC64;
MSYGWYHGNI TRSKAEDLLS QAGKDGSYLV RDSESVCRAY ALCVLNQNCV HTYRILQNAE
HQLSVQASEG VPMRFFTNLV ELIEFYRREN VGLVTHLQYP IEKEEEGPEE PDEEQEPAPP
NVPPRNFAFT PPSETKECQT AIERAPAANA SLLLSETLLQ RFQDTDSRCI PEEHLQAICD
YFSLHIVSDC DMVRTGSQTL PQFKKLLMTL CTGLHRELTR TLPTLESLQV AIDPQLSPGF
KQRSPLPGDS ATNNMVNKLT HLTSMVSNLE EKVKTVLMEG AAVKHRRSLI PPIIFEVKAD
SIGISQKTHL KVDVETGKLI IKKSKDGPDD KFYPSKKILQ LIKSQKFPHK LVIVLETEKE
KTQRKEYVFA DSKKREGFCQ LLQQMKNKHS GQSEPDMLSI FIGTWNMGDA PPPKNITPWF
QCKGQGKTRD DTADYIEHDI YVIGTQEDPL SEKEWTDTLI HSLREITSVE YKVITTQTLW
NIRIVVLAKP EHAHRISHVC TNSVKTGIAN TLGNKGAVGA SFMFNGTSFG FINSHLTSGS
EKKLRRNQNY FNILRFLVLG DKKLSPFNFT HRFNHLFWLG DLNYRLQLPN TEAENIIQKI
KQQQHQELLP HDQLNLERRE SLIFFQFHEE EITFPPTYRY ERGSRERYCY TKQKATGIKY
NLPSWCDRIL WKSYPQMHIL CQSYGCTDDI TTSDHSPVFG TFQVGVTSQF VSKNNPGDSG
DLEAQGHIEL MNCKATLYTK SHTKFYIEFH SPCLENMVKS SEAEDQEGNN GTLVVKFGVL
PKLTPIISDL EYLLDQHLLI CIKSSDTDES YGEGCIALRK EDTEQQFPFC TILTHHGEET
GLFCGEICLP ASGGKQREKL YDFVKIEKDE TVAQKQLKHP YSQSMEQSRI MKSISEKSAM
IARMRAAPET QNSMDHTASV AAISSQAKQS PPTTPPGFRG SEPRQKPGSP VQGRGDTPIT
SPPRTTLSTQ KFSHSNTNRT APAARPQDSL QITVPSDPHE MVDNPLYGPV NNTLYPPTA
